Sandbox Reserved 199: Difference between revisions
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This data suggests an “induced-fit” model of substrate binding and may prove vital to fully understanding RNase 1’s binding specificity for Hcrl; although two residues, <scene name='Sandbox_Reserved_199/2k11_42_43/1'>Pro 42 and Val43</scene>, show much more rigidity and possibly contribute some “lock-and-key” binding interaction. | This data suggests an “induced-fit” model of substrate binding and may prove vital to fully understanding RNase 1’s binding specificity for Hcrl; although two residues, <scene name='Sandbox_Reserved_199/2k11_42_43/1'>Pro 42 and Val43</scene>, show much more rigidity and possibly contribute some “lock-and-key” binding interaction. | ||
[[Image:Kroupa Ribonuclease inhibitor.png|thumb |right |alt=RNase Inhibitor. |Example Ribonuclease inhibitor structure.]] | [[Image:Kroupa Ribonuclease inhibitor.png|thumb |right |alt=RNase Inhibitor. |Example Ribonuclease inhibitor structure<ref>Willow. Top view of ribbon diagram of ribonuclease inhibitor (PDB accession code 2BNH). Made with MOLMOL. 2006. Web. 1 Apr. 2011..</ref>.]] | ||
15N NMR relaxation shows increased T1 values for the residues found in these sheets and loops (0.63-0.64s relative to 0.60s in helices). This suggests greater flexibility in these regions as well. | 15N NMR relaxation shows increased T1 values for the residues found in these sheets and loops (0.63-0.64s relative to 0.60s in helices). This suggests greater flexibility in these regions as well. | ||
